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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Comparative studies of rodent anionic arylsulfatases.

Approximately 25 and 40%, respectively, of murine (Mus musculus) and rat (Rattus norvegicus) hepatic arylsulfatase (EC 3.1.6.1) activity eluted from DEAE-ion exchange resins under high salt conditions. This high salt fraction contained arylsulfatase A and an enzyme which was immunologically similar to arylsulfatase B. The latter enzyme was thermostable, resistant to inhibition by silver, completely inhibited by phosphate, displayed linear kinetics, and had a higher pH optimum than arylsulfatase A. Anionic arylsulfatase B also hydrolyzed chondroitin-4-SO4 heptasaccharide. Sephacryl S-300 gel filtration resolved anionic arylsulfatase B into 55 and 115 kd fractions. Rodent arylsulfatase A activity was grossly underestimated when 4-methyl-umbelliferyl sulfate was employed as substrate.[1]

References

  1. Comparative studies of rodent anionic arylsulfatases. Thompson, D.B., Daniel, W.L., Glaser, J.H. Comp. Biochem. Physiol., B (1985) [Pubmed]
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